Abstract
The glycine receptor is a ligand-gated anion channel protein, providing inhibitory drive within the nervous system. We report here the isolation and functional characterization of a novel α subunit (αZ1) of the glycine receptor from adult zebrafish (Danio rerio) brain. The predicted amino acid sequence is 86%, 81% and 77% identical to mammalian isoforms α1, α3 and α2, respectively. αZ1 exhibits many of the molecular features of mammalian α1, but the sequence patterns in the M4 and C-terminal domains are more similar to α2/α3. Phylogenetic analysis indicates that αZ1 is more closely related to the mammalian α1 subunits, being positioned, however, on a distinct branch. The αZ1 messenger RNA is 9.5 kb, similar to that described previously for α1 messenger RNAs. When expressed in Xenopus oocytes or a human cell line (BOSC 23), αZ1 forms a homomeric receptor which is activated by glycine and antagonized by strychnine. This receptor demonstrates unexpectedly high sensitivity to taurine and can also be activated by GABA. These results are consistent with physiological findings in lamprey and goldfish, and they suggest that this teleost fish glycine receptor displays a lower selectivity to neurotransmitters than that reported for glycine mammalian receptors.
| Original language | English |
|---|---|
| Pages (from-to) | 303-317 |
| Number of pages | 15 |
| Journal | Neuroscience |
| Volume | 90 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 1999 |
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Keywords
- GABA
- Glycine receptor
- Oocyte expression
- Receptor phylogeny
- Taurine
- Zebrafish
ASJC Scopus subject areas
- Neuroscience(all)
Cite this
Cloning, expression and electrophysiological characterization of glycine receptor alpha subunit from zebrafish. / David-Watine, B.; Goblet, C.; De Saint Jan, D.; Fucile, S.; Devignot, V.; Bregestovski, P.; Korn, H.
In: Neuroscience, Vol. 90, No. 1, 1999, p. 303-317.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Cloning, expression and electrophysiological characterization of glycine receptor alpha subunit from zebrafish
AU - David-Watine, B.
AU - Goblet, C.
AU - De Saint Jan, D.
AU - Fucile, S.
AU - Devignot, V.
AU - Bregestovski, P.
AU - Korn, H.
PY - 1999
Y1 - 1999
N2 - The glycine receptor is a ligand-gated anion channel protein, providing inhibitory drive within the nervous system. We report here the isolation and functional characterization of a novel α subunit (αZ1) of the glycine receptor from adult zebrafish (Danio rerio) brain. The predicted amino acid sequence is 86%, 81% and 77% identical to mammalian isoforms α1, α3 and α2, respectively. αZ1 exhibits many of the molecular features of mammalian α1, but the sequence patterns in the M4 and C-terminal domains are more similar to α2/α3. Phylogenetic analysis indicates that αZ1 is more closely related to the mammalian α1 subunits, being positioned, however, on a distinct branch. The αZ1 messenger RNA is 9.5 kb, similar to that described previously for α1 messenger RNAs. When expressed in Xenopus oocytes or a human cell line (BOSC 23), αZ1 forms a homomeric receptor which is activated by glycine and antagonized by strychnine. This receptor demonstrates unexpectedly high sensitivity to taurine and can also be activated by GABA. These results are consistent with physiological findings in lamprey and goldfish, and they suggest that this teleost fish glycine receptor displays a lower selectivity to neurotransmitters than that reported for glycine mammalian receptors.
AB - The glycine receptor is a ligand-gated anion channel protein, providing inhibitory drive within the nervous system. We report here the isolation and functional characterization of a novel α subunit (αZ1) of the glycine receptor from adult zebrafish (Danio rerio) brain. The predicted amino acid sequence is 86%, 81% and 77% identical to mammalian isoforms α1, α3 and α2, respectively. αZ1 exhibits many of the molecular features of mammalian α1, but the sequence patterns in the M4 and C-terminal domains are more similar to α2/α3. Phylogenetic analysis indicates that αZ1 is more closely related to the mammalian α1 subunits, being positioned, however, on a distinct branch. The αZ1 messenger RNA is 9.5 kb, similar to that described previously for α1 messenger RNAs. When expressed in Xenopus oocytes or a human cell line (BOSC 23), αZ1 forms a homomeric receptor which is activated by glycine and antagonized by strychnine. This receptor demonstrates unexpectedly high sensitivity to taurine and can also be activated by GABA. These results are consistent with physiological findings in lamprey and goldfish, and they suggest that this teleost fish glycine receptor displays a lower selectivity to neurotransmitters than that reported for glycine mammalian receptors.
KW - GABA
KW - Glycine receptor
KW - Oocyte expression
KW - Receptor phylogeny
KW - Taurine
KW - Zebrafish
UR - http://www.scopus.com/inward/record.url?scp=0033018543&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033018543&partnerID=8YFLogxK
U2 - 10.1016/S0306-4522(98)00430-8
DO - 10.1016/S0306-4522(98)00430-8
M3 - Article
C2 - 10188956
AN - SCOPUS:0033018543
VL - 90
SP - 303
EP - 317
JO - Neuroscience
JF - Neuroscience
SN - 0306-4522
IS - 1
ER -